1. Volume 86, Issue 5, Pages 835-843 (September 1996)
Structure of the Human Cytomegalovirus Protease Catalytic Domain Reveals a Novel Serine Protease Fold and Catalytic Triad 
Ping Chen, Hideaki Tsuge, Robert J. Almassy, Cindy L. Gribskov, Susumu Katoh, Darin L. Vanderpool, Stephen A. Margosiak, Christopher Pinko, David A. Matthews, Chen-Chen Kan 
Cell 
Volume 86, Issue 5, Pages (September 1996)
DOI: /S (00)

2. Figure 1
View of the HCMV Protease Catalytic Domain Oriented to Highlight the Core β Sheets
Strands are shown in yellow, α-helices in blue, and connecting loops in purple.
Cell  , DOI: ( /S (00) )

3. Figure 2
Secondary Structure Assignments for the HCMV Protease Catalytic Domain and Sequence Alignments for Catalytic Domains of Representative Herpesvirus Proteases
α-helices and β strands are marked as α1–α8 and β1–β8, respectively. HSV-1, herpes simplex-1; HCMV, human cytomegalovirus strain AD169; MCMV, mouse CMV; ColCMV, simian CMV strain Colburn; EBV, Epstein Barr virus.
Cell  , DOI: ( /S (00) )

4. Figure 3
HCMV Protease Catalytic Domain Dimer, Viewed Down the 2-Fold Axis
α-helices are shown in blue, and the two central β sheets are shown in yellow.
Cell  , DOI: ( /S (00) )

5. Figure 4
Stereo View of the HCMV Protease Active Site and Surrounding Residues
The catalytic triad, Arg-165, and Arg-166 are represented with thick bonds. Drawn as spheres with stick bonds is a model peptide showing how the P2 to P1' (Asn-Ala-Ser) portion of a substrate could be positioned within the active-site cleft. A larger sphere marks the iodine position in an iodotyrosine-containing tetrapeptide aldehyde inhibitor bound to the HCMV protease (see text).
Cell  , DOI: ( /S (00) )

6. Figure 5
View of Superposed Catalytic Triads and Oxyanion Binding Sites for HCMV Protease (Yellow), Trypsin (Green), and Subtilisin (Pink)
Cell  , DOI: ( /S (00) )

7. Figure 6
View of the HCMV Protease Dimer Interface Showing Helix α7 from One Protomer and the Molecular Surface of the Other Protomer
Helix α7 sits in a groove formed by five helices from the second subunit, one of which is α7′ (primed secondary structure elements refer to those in the second subunit). The surface of α7′ is directly to the left of α7.
Cell  , DOI: ( /S (00) )

8. Figure 7
A Portion of the Averaged Solvent-Flattened ISAS Electron Density Map Calculated at 2.9 Å Resolution and Contoured at 2.5 σ
Superposed on the density is the final refined model.
Cell  , DOI: ( /S (00) )